MBP-binding DARPins facilitate the crystallization of an MBP fusion protein
| Autor: | Rajesh Gumpena, George T. Lountos, David S. Waugh |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular Protein Conformation alpha-Helical 0301 basic medicine 030103 biophysics Recombinant Fusion Proteins Genetic Vectors Phosphatase Biophysics Gene Expression Crystallography X-Ray medicine.disease_cause Biochemistry Maltose-Binding Proteins law.invention 03 medical and health sciences Maltose-binding protein Structural Biology law Hydrolase Escherichia coli Genetics medicine Humans Protein Interaction Domains and Motifs Amino Acid Sequence Cloning Molecular Crystallization Fusion Binding Sites Sequence Homology Amino Acid biology Chemistry Dual Specificity Phosphatase 1 Condensed Matter Physics Fusion protein 030104 developmental biology Chaperone (protein) biology.protein Protein Conformation beta-Strand Sequence Alignment Molecular Chaperones Protein Binding |
| Zdroj: | Acta Crystallographica Section F Structural Biology Communications. 74:549-557 |
| ISSN: | 2053-230X |
| DOI: | 10.1107/s2053230x18009901 |
| Popis: | The production of high-quality crystals is the main bottleneck in determining the structures of proteins using X-ray crystallography. In addition to being recognized as a very effective solubility-enhancing fusion partner,Escherichia colimaltose-binding protein (MBP) has also been successfully employed as a `fixed-arm' crystallization chaperone in more than 100 cases. Here, it is reported that designed ankyrin-repeat proteins (DARPins) that bind with high affinity to MBP can promote the crystallization of an MBP fusion protein when the fusion protein alone fails to produce diffraction-quality crystals. As a proof of principle, three different co-crystal structures of MBP fused to the catalytic domain of human dual-specificity phosphatase 1 in complex with DARPins are reported. |
| Databáze: | OpenAIRE |
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